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6KTQ

Crystal structure of catalytic domain of homocitrate synthase from Sulfolobus acidocaldarius (SaHCS(dRAM)) in complex with alpha-ketoglutarate/Zn2+/CoA

Summary for 6KTQ
Entry DOI10.2210/pdb6ktq/pdb
DescriptorHomocitrate synthase, ZINC ION, 2-OXOGLUTARIC ACID, ... (7 entities in total)
Functional Keywordshomocitrate synthase, sulfolobus acidocaldarius, complex, biosynthetic protein, lyase
Biological sourceSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Total number of polymer chains2
Total formula weight94392.97
Authors
Suzuki, T.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2019-08-28, release date: 2020-09-02, Last modification date: 2023-11-22)
Primary citationSuzuki, T.,Tomita, T.,Hirayama, K.,Suzuki, M.,Kuzuyama, T.,Nishiyama, M.
Involvement of subdomain II in the recognition of acetyl-CoA revealed by the crystal structure of homocitrate synthase from Sulfolobus acidocaldarius.
Febs J., 288:1975-1988, 2021
Cited by
PubMed Abstract: Homocitrate synthase (HCS) catalyzes the aldol condensation of α-ketoglutarate and acetyl coenzyme A to form homocitrate, which is the first committed step of lysine biosynthesis through the α-aminoadipate pathway in yeast, fungi, and some prokaryotes. We determined the crystal structure of a truncated form of HCS from a hyperthermophilic acidophilic archaeon, Sulfolobus acidocaldarius, which lacks the RAM (Regulation of amino acid metabolism) domain at the C terminus serving as the regulatory domain for the feedback inhibition by lysine, in complex with α-ketoglutarate, Mg , and CoA. This structure coupled with mutational analysis revealed that a subdomain, subdomain II, connecting the N-terminal catalytic domain and C-terminal RAM domain is involved in the recognition of acetyl-CoA. This is the first structural evidence of the function of subdomain II in the related enzyme family, which will lead to a better understanding of the catalytic mechanism of HCS. DATABASES: Structural data are available in the RCSB PDB database under the accession number 6KTQ.
PubMed: 32897601
DOI: 10.1111/febs.15527
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.98 Å)
Structure validation

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